G3V801 (NETR_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neurotrypsin
EC=3.4.21.-

Alternative name(s):
Serine protease 12

Gene names

Name:

Prss12

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	761 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations By similarity.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 kringle domain. Contains 1 peptidase S1 domain. Contains 3 SRCR domains.

Ontologies

Keywords
Cellular component	Secreted
Domain	Kringle Repeat Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	exocytosis Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW zymogen activation Inferred from electronic annotation. Source: Compara
Cellular_component	axon Inferred from sequence or structural similarity. Source: UniProtKB cytoplasmic vesicle Inferred from electronic annotation. Source: Compara dendrite Inferred from electronic annotation. Source: Compara extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB synaptic cleft Inferred from electronic annotation. Source: Compara terminal bouton Inferred from electronic annotation. Source: Compara
Molecular_function	scavenger receptor activity Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 761

740

Neurotrypsin

PRO_0000416843

Regions

Domain

85 – 157

73

Kringle

Domain

166 – 267

102

SRCR 1

Domain

273 – 373

101

SRCR 2

Domain

386 – 487

102

SRCR 3

Domain

517 – 760

244

Peptidase S1

Region

505 – 516

12

Zymogen activation region By similarity

Sites

Active site

562

1

Charge relay system By similarity

Active site

612

1

Charge relay system By similarity

Active site

711

1

Charge relay system By similarity

Site

516 – 517

2

Reactive bond homolog Potential

Amino acid modifications

Glycosylation

93

1

N-linked (GlcNAc...) Potential

Glycosylation

521

1

N-linked (GlcNAc...) Potential

Glycosylation

569

1

N-linked (GlcNAc...) Potential

Disulfide bond

85 ↔ 157

Ref.4

Disulfide bond

101 ↔ 141

Ref.4

Disulfide bond

130 ↔ 155

Ref.4

Disulfide bond

191 ↔ 255

By similarity

Disulfide bond

204 ↔ 265

By similarity

Disulfide bond

235 ↔ 245

By similarity

Disulfide bond

298 ↔ 361

By similarity

Disulfide bond

311 ↔ 371

By similarity

Disulfide bond

341 ↔ 351

By similarity

Disulfide bond

411 ↔ 475

By similarity

Disulfide bond

424 ↔ 485

By similarity

Disulfide bond

455 ↔ 465

By similarity

Disulfide bond

505 ↔ 636

Potential

Disulfide bond

547 ↔ 563

By similarity

Disulfide bond

651 ↔ 717

By similarity

Disulfide bond

680 ↔ 694

By similarity

Disulfide bond

707 ↔ 736

By similarity

Experimental info

Sequence conflict

134

1

G → D in CAC35028. Ref.1

Sequence conflict

404

1

S → N in CAC35028. Ref.1

Sequence conflict

515

1

K → T in CAC35028. Ref.1

Sequence conflict

565

1

K → T in CAC35028. Ref.1

Sequence conflict

588

1

E → G in CAC35028. Ref.1

Sequence conflict

592

1

E → D in CAC35028. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

761

Helix Strand Turn

Details...

Beta strand

92 – 95

4

Beta strand

98 – 101

4

Helix

104 – 106

3

Helix

119 – 121

3

Beta strand

131 – 134

4

Turn

135 – 137

3

Beta strand

138 – 144

7

Beta strand

150 – 154

5

Beta strand

156 – 158

3

Sequences

	Sequence		Length	Mass (Da)
	G3V801 [UniParc]. Last modified November 16, 2011. Version 1. Checksum: 215EE73A3CE468EA	FASTA	761	84,220
	10 20 30 40 50 60 MALARCVLAV ILGVLSEVAR ADPVLHSPLH RPHPSPPRSQ HAHYLPSSRR PPRTPRFPLP 70 80 90 100 110 120 PRAPAAQRPQ LLSTRHTPPT ISRRCGAGEP WGNATNLGVP CLHWDEVPPF LERSPPASWA 130 140 150 160 170 180 ELRGQPHNFC RSPGGAGRPW CFYRNAQGKV DWGYCDCGQG PALPVIRLVG GKSGHEGRVE 190 200 210 220 230 240 LYHAGQWGTI CDDQWDDADA EVICRQLGLS GIAKAWHQAH FGEGSGPILL DEVRCTGNEL 250 260 270 280 290 300 SIEQCPKSSW GEHNCGHKED AGVSCAPLTD GVIRLSGGKS VHEGRLEVYY RGQWGTVCDD 310 320 330 340 350 360 GWTEMNTYVA CRLLGFKYGK QSSVNHFEGS SRPIWLDDVS CSGKEASFIQ CSRRQWGRHD 370 380 390 400 410 420 CSHREDVGLT CYPDSDGHRL SPGFPIRLMD GENKREGRVE VFVSGQWGTI CDDGWTDKHA 430 440 450 460 470 480 AVICRQLGYK GPARARTMAY FGEGKGPIHM DNVKCTGNEK ALADCVKQDI GRHNCRHSED 490 500 510 520 530 540 AGVICDYYEK KTSGHGNKET LSSGCGLRLL HRRQKRIIGG NNSLRGAWPW QASLRLKSTH 550 560 570 580 590 600 GDGRLLCGAT LLSSCWVLTA AHCFKRYGNN SRSYAVRVGD YHTLVPEEFE QEIGVQQIVI 610 620 630 640 650 660 HRNYRPDSSD YDIALVRLQG SGEQCARLST HVLPACLPLW RERPQKTASN CHITGWGDTG 670 680 690 700 710 720 RAYSRTLQQA AVPLLPKRFC KERYKGLFTG RMLCAGNLQE DNRVDSCQGD SGGPLMCEKP 730 740 750 760 DETWVVYGVT SWGYGCGIKD TPGVYTRVPA FVPWIKSVTS L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of the cDNA encoding rat neurotrypsin." Hintsch G., Sonderegger P. Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[4]	"NMR solution structure of the neurotrypsin Kringle domain." Ozhogina O.A., Grishaev A., Bominaar E.L., Patthy L., Trexler M., Llinas M. Biochemistry 47:12290-12298(2008) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 84-160, PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, DISULFIDE BOND.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ311671 mRNA. Translation: CAC35028.2.
CH473952 Genomic DNA. Translation: EDL82129.1.

IPI

IPI00195021.

RefSeq

NP_445956.1. NM_053504.1.

UniGene

Rn.86653.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K4R	NMR	-	A	84-160	[»]
2K51	NMR	-	A	84-160	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

10116.ENSRNOP00000021116.

Protein family/group databases

MEROPS

S01.237.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000021116; ENSRNOP00000021116; ENSRNOG00000015353.

GeneID

85266.

KEGG

rno:85266.

Organism-specific databases

CTD

8492.

RGD

69238. Prss12.

Phylogenomic databases

eggNOG

COG5640.

GeneTree

ENSGT00700000104326.

HOGENOM

HOG000113767.

KO

K09624.

OMA

DWGYCDC.

OrthoDB

EOG46WZ7R.

Family and domain databases

Gene3D

2.40.20.10. 1 hit.

InterPro

IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR001190. Srcr_rcpt.
IPR017448. Srcr_rcpt-rel.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]

Pfam

PF00051. Kringle. 1 hit.
PF00530. SRCR. 3 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00722. CHYMOTRYPSIN.
PR00258. SPERACTRCPTR.

SMART

SM00130. KR. 1 hit.
SM00202. SR. 3 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]

SUPFAM

SSF57440. Kringle-like. 1 hit.
SSF50494. Pept_Ser_Cys. 1 hit.
SSF56487. Srcr_receptor. 3 hits.

PROSITE

PS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_2. 1 hit.
PS00420. SRCR_1. 3 hits.
PS50287. SRCR_2. 3 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

617408.

Entry information

Entry name

NETR_RAT

Accession

Primary (citable) accession number: G3V801
Secondary accession number(s): Q99JC8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2012
Last sequence update:	November 16, 2011
Last modified:	April 3, 2013
This is version 17 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program